1fhw: Difference between revisions

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 <StructureSection load='1fhw' size='340' side='right'caption='[[1fhw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fhw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FHW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fhw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I5P:INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE'>I5P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fhx|1fhx]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I5P:INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE'>I5P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhw OCA], [http://pdbe.org/1fhw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fhw RCSB], [http://www.ebi.ac.uk/pdbsum/1fhw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhw ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhw OCA], [https://pdbe.org/1fhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhw RCSB], [https://www.ebi.ac.uk/pdbsum/1fhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhw ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CYH3_MOUSE CYH3_MOUSE] Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP.<ref>PMID:18042453</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fhw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal-dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two different PH domains bound to Ins(1,3,4,5)P4, the head group of the major PI 3-K product PtdIns(3,4,5)P3. One of these PH domains (from Grp1) is PtdIns(3,4,5)P3 specific, while the other (from DAPP1/PHISH) binds strongly to both PtdIns(3,4,5)P3 and its 5'-dephosphorylation product, PtdIns(3,4)P2. Comparison of the two structures provides an explanation for the distinct phosphoinositide specificities of the two PH domains and allows us to predict the 3-phosphoinositide selectivity of uncharacterized PH domains.
-Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains.,Ferguson KM, Kavran JM, Sankaran VG, Fournier E, Isakoff SJ, Skolnik EY, Lemmon MA Mol Cell. 2000 Aug;6(2):373-84. PMID:10983984<ref>PMID:10983984</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fhw" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 32: / Line 25: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Ferguson, K M]]
+[[Category: Ferguson KM]]
-[[Category: Fournier, E]]
+[[Category: Fournier E]]
-[[Category: Isakoff, S J]]
+[[Category: Isakoff SJ]]
-[[Category: Kavran, J M]]
+[[Category: Kavran JM]]
-[[Category: Lemmon, M A]]
+[[Category: Lemmon MA]]
-[[Category: Sankaran, V G]]
+[[Category: Sankaran VG]]
-[[Category: Skolnik, E Y]]
+[[Category: Skolnik EY]]
-[[Category: 3-phosphoinositide]]
-[[Category: Guanine nucleotide exchange factor]]
-[[Category: Inositol tetrakisphosphate signal transduction protein]]
-[[Category: Pleckstrin]]
-[[Category: Signaling protein]]